Functional Information from GO Data
| Chain | GOid | namespace | contents |
| AA | 0005506 | molecular_function | iron ion binding |
| AA | 0009055 | molecular_function | electron transfer activity |
| AA | 0009523 | cellular_component | photosystem II |
| AA | 0009635 | biological_process | response to herbicide |
| AA | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| AA | 0010242 | molecular_function | oxygen evolving activity |
| AA | 0015979 | biological_process | photosynthesis |
| AA | 0016168 | molecular_function | chlorophyll binding |
| AA | 0016491 | molecular_function | oxidoreductase activity |
| AA | 0016682 | molecular_function | oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor |
| AA | 0019684 | biological_process | photosynthesis, light reaction |
| AA | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| AA | 0042651 | cellular_component | thylakoid membrane |
| AA | 0046872 | molecular_function | metal ion binding |
| AB | 0009521 | cellular_component | photosystem |
| AB | 0009523 | cellular_component | photosystem II |
| AB | 0009767 | biological_process | photosynthetic electron transport chain |
| AB | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| AB | 0015979 | biological_process | photosynthesis |
| AB | 0016020 | cellular_component | membrane |
| AB | 0016168 | molecular_function | chlorophyll binding |
| AB | 0019684 | biological_process | photosynthesis, light reaction |
| AB | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| AB | 0042651 | cellular_component | thylakoid membrane |
| AC | 0005737 | cellular_component | cytoplasm |
| AC | 0009521 | cellular_component | photosystem |
| AC | 0009523 | cellular_component | photosystem II |
| AC | 0009767 | biological_process | photosynthetic electron transport chain |
| AC | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| AC | 0015979 | biological_process | photosynthesis |
| AC | 0016020 | cellular_component | membrane |
| AC | 0016168 | molecular_function | chlorophyll binding |
| AC | 0019684 | biological_process | photosynthesis, light reaction |
| AC | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| AC | 0042651 | cellular_component | thylakoid membrane |
| AC | 0046872 | molecular_function | metal ion binding |
| AD | 0005506 | molecular_function | iron ion binding |
| AD | 0005737 | cellular_component | cytoplasm |
| AD | 0009055 | molecular_function | electron transfer activity |
| AD | 0009523 | cellular_component | photosystem II |
| AD | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| AD | 0010242 | molecular_function | oxygen evolving activity |
| AD | 0015979 | biological_process | photosynthesis |
| AD | 0016020 | cellular_component | membrane |
| AD | 0016168 | molecular_function | chlorophyll binding |
| AD | 0016491 | molecular_function | oxidoreductase activity |
| AD | 0019684 | biological_process | photosynthesis, light reaction |
| AD | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| AD | 0042651 | cellular_component | thylakoid membrane |
| AD | 0046872 | molecular_function | metal ion binding |
| AE | 0005506 | molecular_function | iron ion binding |
| AE | 0005737 | cellular_component | cytoplasm |
| AE | 0009055 | molecular_function | electron transfer activity |
| AE | 0009523 | cellular_component | photosystem II |
| AE | 0009539 | cellular_component | photosystem II reaction center |
| AE | 0009767 | biological_process | photosynthetic electron transport chain |
| AE | 0015979 | biological_process | photosynthesis |
| AE | 0016020 | cellular_component | membrane |
| AE | 0019684 | biological_process | photosynthesis, light reaction |
| AE | 0020037 | molecular_function | heme binding |
| AE | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| AE | 0042651 | cellular_component | thylakoid membrane |
| AE | 0046872 | molecular_function | metal ion binding |
| AF | 0005506 | molecular_function | iron ion binding |
| AF | 0005737 | cellular_component | cytoplasm |
| AF | 0009055 | molecular_function | electron transfer activity |
| AF | 0009523 | cellular_component | photosystem II |
| AF | 0009539 | cellular_component | photosystem II reaction center |
| AF | 0009767 | biological_process | photosynthetic electron transport chain |
| AF | 0015979 | biological_process | photosynthesis |
| AF | 0016020 | cellular_component | membrane |
| AF | 0019684 | biological_process | photosynthesis, light reaction |
| AF | 0020037 | molecular_function | heme binding |
| AF | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| AF | 0042651 | cellular_component | thylakoid membrane |
| AF | 0046872 | molecular_function | metal ion binding |
| AH | 0009523 | cellular_component | photosystem II |
| AH | 0015979 | biological_process | photosynthesis |
| AH | 0016020 | cellular_component | membrane |
| AH | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| AH | 0042301 | molecular_function | phosphate ion binding |
| AH | 0042651 | cellular_component | thylakoid membrane |
| AH | 0050821 | biological_process | protein stabilization |
| AI | 0005737 | cellular_component | cytoplasm |
| AI | 0009523 | cellular_component | photosystem II |
| AI | 0009539 | cellular_component | photosystem II reaction center |
| AI | 0015979 | biological_process | photosynthesis |
| AI | 0016020 | cellular_component | membrane |
| AI | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| AI | 0042651 | cellular_component | thylakoid membrane |
| AJ | 0009523 | cellular_component | photosystem II |
| AJ | 0009539 | cellular_component | photosystem II reaction center |
| AJ | 0015979 | biological_process | photosynthesis |
| AJ | 0016020 | cellular_component | membrane |
| AJ | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| AJ | 0042651 | cellular_component | thylakoid membrane |
| AK | 0009523 | cellular_component | photosystem II |
| AK | 0009539 | cellular_component | photosystem II reaction center |
| AK | 0015979 | biological_process | photosynthesis |
| AL | 0005737 | cellular_component | cytoplasm |
| AL | 0009523 | cellular_component | photosystem II |
| AL | 0009539 | cellular_component | photosystem II reaction center |
| AL | 0015979 | biological_process | photosynthesis |
| AL | 0016020 | cellular_component | membrane |
| AL | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| AL | 0042651 | cellular_component | thylakoid membrane |
| AM | 0005737 | cellular_component | cytoplasm |
| AM | 0009523 | cellular_component | photosystem II |
| AM | 0015979 | biological_process | photosynthesis |
| AM | 0016020 | cellular_component | membrane |
| AM | 0019684 | biological_process | photosynthesis, light reaction |
| AM | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| AM | 0042651 | cellular_component | thylakoid membrane |
| AO | 0009654 | cellular_component | photosystem II oxygen evolving complex |
| AO | 0010207 | biological_process | photosystem II assembly |
| AO | 0010242 | molecular_function | oxygen evolving activity |
| AO | 0042549 | biological_process | photosystem II stabilization |
| AT | 0009523 | cellular_component | photosystem II |
| AT | 0009539 | cellular_component | photosystem II reaction center |
| AT | 0015979 | biological_process | photosynthesis |
| AT | 0016020 | cellular_component | membrane |
| AT | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| AT | 0042651 | cellular_component | thylakoid membrane |
| AU | 0009523 | cellular_component | photosystem II |
| AU | 0009654 | cellular_component | photosystem II oxygen evolving complex |
| AU | 0015979 | biological_process | photosynthesis |
| AU | 0019898 | cellular_component | extrinsic component of membrane |
| AU | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| AU | 0042549 | biological_process | photosystem II stabilization |
| AU | 0042651 | cellular_component | thylakoid membrane |
| AV | 0005506 | molecular_function | iron ion binding |
| AV | 0009055 | molecular_function | electron transfer activity |
| AV | 0009523 | cellular_component | photosystem II |
| AV | 0015979 | biological_process | photosynthesis |
| AV | 0019684 | biological_process | photosynthesis, light reaction |
| AV | 0020037 | molecular_function | heme binding |
| AV | 0022904 | biological_process | respiratory electron transport chain |
| AV | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| AV | 0042651 | cellular_component | thylakoid membrane |
| AV | 0046872 | molecular_function | metal ion binding |
| AX | 0009523 | cellular_component | photosystem II |
| AX | 0015979 | biological_process | photosynthesis |
| AX | 0016020 | cellular_component | membrane |
| AX | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| AX | 0042651 | cellular_component | thylakoid membrane |
| Ay | 0009523 | cellular_component | photosystem II |
| Ay | 0015979 | biological_process | photosynthesis |
| Ay | 0016020 | cellular_component | membrane |
| Ay | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| Ay | 0042651 | cellular_component | thylakoid membrane |
| AZ | 0009523 | cellular_component | photosystem II |
| AZ | 0009539 | cellular_component | photosystem II reaction center |
| AZ | 0015979 | biological_process | photosynthesis |
| AZ | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| AZ | 0042549 | biological_process | photosystem II stabilization |
| AZ | 0042651 | cellular_component | thylakoid membrane |
| BA | 0005506 | molecular_function | iron ion binding |
| BA | 0009055 | molecular_function | electron transfer activity |
| BA | 0009523 | cellular_component | photosystem II |
| BA | 0009635 | biological_process | response to herbicide |
| BA | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| BA | 0010242 | molecular_function | oxygen evolving activity |
| BA | 0015979 | biological_process | photosynthesis |
| BA | 0016168 | molecular_function | chlorophyll binding |
| BA | 0016491 | molecular_function | oxidoreductase activity |
| BA | 0016682 | molecular_function | oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor |
| BA | 0019684 | biological_process | photosynthesis, light reaction |
| BA | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| BA | 0042651 | cellular_component | thylakoid membrane |
| BA | 0046872 | molecular_function | metal ion binding |
| BB | 0009521 | cellular_component | photosystem |
| BB | 0009523 | cellular_component | photosystem II |
| BB | 0009767 | biological_process | photosynthetic electron transport chain |
| BB | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| BB | 0015979 | biological_process | photosynthesis |
| BB | 0016020 | cellular_component | membrane |
| BB | 0016168 | molecular_function | chlorophyll binding |
| BB | 0019684 | biological_process | photosynthesis, light reaction |
| BB | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| BB | 0042651 | cellular_component | thylakoid membrane |
| BC | 0005737 | cellular_component | cytoplasm |
| BC | 0009521 | cellular_component | photosystem |
| BC | 0009523 | cellular_component | photosystem II |
| BC | 0009767 | biological_process | photosynthetic electron transport chain |
| BC | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| BC | 0015979 | biological_process | photosynthesis |
| BC | 0016020 | cellular_component | membrane |
| BC | 0016168 | molecular_function | chlorophyll binding |
| BC | 0019684 | biological_process | photosynthesis, light reaction |
| BC | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| BC | 0042651 | cellular_component | thylakoid membrane |
| BC | 0046872 | molecular_function | metal ion binding |
| BD | 0005506 | molecular_function | iron ion binding |
| BD | 0005737 | cellular_component | cytoplasm |
| BD | 0009055 | molecular_function | electron transfer activity |
| BD | 0009523 | cellular_component | photosystem II |
| BD | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| BD | 0010242 | molecular_function | oxygen evolving activity |
| BD | 0015979 | biological_process | photosynthesis |
| BD | 0016020 | cellular_component | membrane |
| BD | 0016168 | molecular_function | chlorophyll binding |
| BD | 0016491 | molecular_function | oxidoreductase activity |
| BD | 0019684 | biological_process | photosynthesis, light reaction |
| BD | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| BD | 0042651 | cellular_component | thylakoid membrane |
| BD | 0046872 | molecular_function | metal ion binding |
| BE | 0005506 | molecular_function | iron ion binding |
| BE | 0005737 | cellular_component | cytoplasm |
| BE | 0009055 | molecular_function | electron transfer activity |
| BE | 0009523 | cellular_component | photosystem II |
| BE | 0009539 | cellular_component | photosystem II reaction center |
| BE | 0009767 | biological_process | photosynthetic electron transport chain |
| BE | 0015979 | biological_process | photosynthesis |
| BE | 0016020 | cellular_component | membrane |
| BE | 0019684 | biological_process | photosynthesis, light reaction |
| BE | 0020037 | molecular_function | heme binding |
| BE | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| BE | 0042651 | cellular_component | thylakoid membrane |
| BE | 0046872 | molecular_function | metal ion binding |
| BF | 0005506 | molecular_function | iron ion binding |
| BF | 0005737 | cellular_component | cytoplasm |
| BF | 0009055 | molecular_function | electron transfer activity |
| BF | 0009523 | cellular_component | photosystem II |
| BF | 0009539 | cellular_component | photosystem II reaction center |
| BF | 0009767 | biological_process | photosynthetic electron transport chain |
| BF | 0015979 | biological_process | photosynthesis |
| BF | 0016020 | cellular_component | membrane |
| BF | 0019684 | biological_process | photosynthesis, light reaction |
| BF | 0020037 | molecular_function | heme binding |
| BF | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| BF | 0042651 | cellular_component | thylakoid membrane |
| BF | 0046872 | molecular_function | metal ion binding |
| BH | 0009523 | cellular_component | photosystem II |
| BH | 0015979 | biological_process | photosynthesis |
| BH | 0016020 | cellular_component | membrane |
| BH | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| BH | 0042301 | molecular_function | phosphate ion binding |
| BH | 0042651 | cellular_component | thylakoid membrane |
| BH | 0050821 | biological_process | protein stabilization |
| BI | 0005737 | cellular_component | cytoplasm |
| BI | 0009523 | cellular_component | photosystem II |
| BI | 0009539 | cellular_component | photosystem II reaction center |
| BI | 0015979 | biological_process | photosynthesis |
| BI | 0016020 | cellular_component | membrane |
| BI | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| BI | 0042651 | cellular_component | thylakoid membrane |
| BJ | 0009523 | cellular_component | photosystem II |
| BJ | 0009539 | cellular_component | photosystem II reaction center |
| BJ | 0015979 | biological_process | photosynthesis |
| BJ | 0016020 | cellular_component | membrane |
| BJ | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| BJ | 0042651 | cellular_component | thylakoid membrane |
| BK | 0009523 | cellular_component | photosystem II |
| BK | 0009539 | cellular_component | photosystem II reaction center |
| BK | 0015979 | biological_process | photosynthesis |
| BL | 0005737 | cellular_component | cytoplasm |
| BL | 0009523 | cellular_component | photosystem II |
| BL | 0009539 | cellular_component | photosystem II reaction center |
| BL | 0015979 | biological_process | photosynthesis |
| BL | 0016020 | cellular_component | membrane |
| BL | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| BL | 0042651 | cellular_component | thylakoid membrane |
| BM | 0005737 | cellular_component | cytoplasm |
| BM | 0009523 | cellular_component | photosystem II |
| BM | 0015979 | biological_process | photosynthesis |
| BM | 0016020 | cellular_component | membrane |
| BM | 0019684 | biological_process | photosynthesis, light reaction |
| BM | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| BM | 0042651 | cellular_component | thylakoid membrane |
| BO | 0009654 | cellular_component | photosystem II oxygen evolving complex |
| BO | 0010207 | biological_process | photosystem II assembly |
| BO | 0010242 | molecular_function | oxygen evolving activity |
| BO | 0042549 | biological_process | photosystem II stabilization |
| BT | 0009523 | cellular_component | photosystem II |
| BT | 0009539 | cellular_component | photosystem II reaction center |
| BT | 0015979 | biological_process | photosynthesis |
| BT | 0016020 | cellular_component | membrane |
| BT | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| BT | 0042651 | cellular_component | thylakoid membrane |
| BU | 0009523 | cellular_component | photosystem II |
| BU | 0009654 | cellular_component | photosystem II oxygen evolving complex |
| BU | 0015979 | biological_process | photosynthesis |
| BU | 0019898 | cellular_component | extrinsic component of membrane |
| BU | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| BU | 0042549 | biological_process | photosystem II stabilization |
| BU | 0042651 | cellular_component | thylakoid membrane |
| BV | 0005506 | molecular_function | iron ion binding |
| BV | 0009055 | molecular_function | electron transfer activity |
| BV | 0009523 | cellular_component | photosystem II |
| BV | 0015979 | biological_process | photosynthesis |
| BV | 0019684 | biological_process | photosynthesis, light reaction |
| BV | 0020037 | molecular_function | heme binding |
| BV | 0022904 | biological_process | respiratory electron transport chain |
| BV | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| BV | 0042651 | cellular_component | thylakoid membrane |
| BV | 0046872 | molecular_function | metal ion binding |
| BX | 0009523 | cellular_component | photosystem II |
| BX | 0015979 | biological_process | photosynthesis |
| BX | 0016020 | cellular_component | membrane |
| BX | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| BX | 0042651 | cellular_component | thylakoid membrane |
| By | 0009523 | cellular_component | photosystem II |
| By | 0015979 | biological_process | photosynthesis |
| By | 0016020 | cellular_component | membrane |
| By | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| By | 0042651 | cellular_component | thylakoid membrane |
| BZ | 0009523 | cellular_component | photosystem II |
| BZ | 0009539 | cellular_component | photosystem II reaction center |
| BZ | 0015979 | biological_process | photosynthesis |
| BZ | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| BZ | 0042549 | biological_process | photosystem II stabilization |
| BZ | 0042651 | cellular_component | thylakoid membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue FE2 AA 401 |
| Chain | Residue |
| AA | HIS215 |
| AA | HIS272 |
| AD | HIS214 |
| AD | HIS268 |
| AD | BCT401 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | binding site for residue CLA AA 402 |
| Chain | Residue |
| AA | VAL157 |
| AA | MET183 |
| AA | PHE186 |
| AA | GLN187 |
| AA | LEU193 |
| AA | HIS198 |
| AA | GLY201 |
| AA | VAL205 |
| AA | THR286 |
| AA | ILE290 |
| AA | CLA403 |
| AA | CLA404 |
| AA | PHO405 |
| AD | LEU182 |
| AD | CLA402 |
| AT | PHE17 |
| AA | PHE119 |
| AA | TYR147 |
| AA | SER153 |
| AA | ALA154 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | binding site for residue CLA AA 403 |
| Chain | Residue |
| AA | THR45 |
| AA | VAL157 |
| AA | PHE158 |
| AA | MET172 |
| AA | ILE176 |
| AA | THR179 |
| AA | MET183 |
| AA | CLA402 |
| AA | PHO405 |
| AA | LMG413 |
| AD | MET198 |
| AD | VAL201 |
| AD | ALA202 |
| AD | GLY206 |
| AD | CLA402 |
| AD | PL9405 |
| AL | LEU30 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue CLA AA 404 |
| Chain | Residue |
| AA | GLN199 |
| AA | VAL202 |
| AA | ALA203 |
| AA | GLY207 |
| AA | TRP278 |
| AA | CLA402 |
| AD | PHE157 |
| AD | VAL175 |
| AD | ILE178 |
| AD | PHE179 |
| AD | LEU182 |
| AD | CLA402 |
| AD | PHO403 |
| AD | LMG407 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | binding site for residue PHO AA 405 |
| Chain | Residue |
| AA | LEU41 |
| AA | ALA44 |
| AA | THR45 |
| AA | ILE115 |
| AA | TYR126 |
| AA | GLN130 |
| AA | ALA146 |
| AA | TYR147 |
| AA | PRO150 |
| AA | LEU174 |
| AA | GLY175 |
| AA | VAL283 |
| AA | CLA402 |
| AA | CLA403 |
| AD | LEU205 |
| AD | ALA208 |
| AD | LEU209 |
| AD | ILE213 |
| AD | TRP253 |
| AD | PHE257 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue CLA AA 406 |
| Chain | Residue |
| AA | ILE36 |
| AA | PRO39 |
| AA | THR40 |
| AA | PHE93 |
| AA | PRO95 |
| AA | ILE96 |
| AA | TRP97 |
| AA | LEU114 |
| AA | PHE117 |
| AA | HIS118 |
| AA | LEU121 |
| AA | DGD410 |
| AI | TYR9 |
| AI | VAL12 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | binding site for residue PL9 AA 407 |
| Chain | Residue |
| AA | PHE274 |
| AD | PHE38 |
| AD | ALA41 |
| AD | TYR42 |
| AD | LEU45 |
| AF | ALA22 |
| AF | THR25 |
| AJ | PL9101 |
| AA | PHE211 |
| AA | MET214 |
| AA | HIS215 |
| AA | LEU218 |
| AA | HIS252 |
| AA | PHE255 |
| AA | SER264 |
| AA | PHE265 |
| AA | LEU271 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue OEC AA 408 |
| Chain | Residue |
| AA | ASP170 |
| AA | GLU189 |
| AA | HIS332 |
| AA | GLU333 |
| AA | ASP342 |
| AA | ALA344 |
| AC | GLU354 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue BCR AA 409 |
| Chain | Residue |
| AA | ILE38 |
| AA | LEU42 |
| AA | ALA43 |
| AA | ALA51 |
| AA | TRP105 |
| AA | SQD415 |
| AI | PHE15 |
| site_id | AD1 |
| Number of Residues | 15 |
| Details | binding site for residue DGD AA 410 |
| Chain | Residue |
| AA | PHE93 |
| AA | PRO95 |
| AA | TRP97 |
| AA | GLU98 |
| AA | CLA406 |
| AC | LEU214 |
| AC | LYS215 |
| AC | SER216 |
| AC | PRO217 |
| AC | PHE218 |
| AC | TRP223 |
| AC | PHE284 |
| AI | LYS5 |
| AI | TYR9 |
| AO | GLY38 |
| site_id | AD2 |
| Number of Residues | 16 |
| Details | binding site for residue LHG AA 411 |
| Chain | Residue |
| AA | ARG140 |
| AA | TRP142 |
| AA | PHE273 |
| AA | SQD412 |
| AC | TRP36 |
| AC | TRP443 |
| AC | ARG447 |
| AC | CLA504 |
| AC | CLA508 |
| AC | CLA510 |
| AD | GLU219 |
| AD | ASN220 |
| AD | ALA229 |
| AD | SER230 |
| AD | THR231 |
| AD | PHE232 |
| site_id | AD3 |
| Number of Residues | 12 |
| Details | binding site for residue SQD AA 412 |
| Chain | Residue |
| AA | ASN267 |
| AA | SER270 |
| AA | PHE273 |
| AA | LHG411 |
| AC | TRP36 |
| AC | CLA508 |
| AC | DGD518 |
| AC | LHG521 |
| AD | PHE232 |
| AD | ARG233 |
| AJ | PL9101 |
| AK | PHE37 |
| site_id | AD4 |
| Number of Residues | 17 |
| Details | binding site for residue LMG AA 413 |
| Chain | Residue |
| AA | SER232 |
| AA | ASN234 |
| AA | CLA403 |
| AB | TRP5 |
| AB | TYR6 |
| AB | CLA611 |
| AB | LMG621 |
| AD | TRP266 |
| AD | PHE273 |
| AL | GLU11 |
| AL | LEU12 |
| AL | ASN13 |
| AL | SER16 |
| AL | LEU19 |
| AL | GLY20 |
| AL | LEU22 |
| AL | VAL26 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue CL AA 414 |
| Chain | Residue |
| AA | HIS332 |
| AA | GLU333 |
| AD | LYS317 |
| site_id | AD6 |
| Number of Residues | 12 |
| Details | binding site for residue SQD AA 415 |
| Chain | Residue |
| AA | TRP20 |
| AA | ASN26 |
| AA | ARG27 |
| AA | LEU28 |
| AA | VAL30 |
| AA | LEU42 |
| AA | BCR409 |
| AT | BCR102 |
| BB | TRP113 |
| BB | TYR117 |
| BB | CLA619 |
| BB | BCR622 |
| site_id | AD7 |
| Number of Residues | 12 |
| Details | binding site for residue LMG AA 416 |
| Chain | Residue |
| AA | LEU72 |
| AA | TYR73 |
| AA | LEU102 |
| AA | ASP103 |
| AD | ARG304 |
| AO | GLY138 |
| AT | LMT101 |
| BB | ALA43 |
| BB | TRP75 |
| BB | SER76 |
| BB | TRP78 |
| BB | LEU98 |
| site_id | AD8 |
| Number of Residues | 9 |
| Details | binding site for residue CLA AB 601 |
| Chain | Residue |
| AB | TRP185 |
| AB | PRO187 |
| AB | PHE190 |
| AB | ILE207 |
| AB | VAL208 |
| AB | CLA602 |
| AH | PHE41 |
| AH | ILE44 |
| AH | BCR101 |
| site_id | AD9 |
| Number of Residues | 22 |
| Details | binding site for residue CLA AB 602 |
| Chain | Residue |
| AB | GLU184 |
| AB | GLY189 |
| AB | PHE190 |
| AB | GLY197 |
| AB | ALA200 |
| AB | HIS201 |
| AB | ALA205 |
| AB | VAL208 |
| AB | PHE246 |
| AB | PHE247 |
| AB | PHE250 |
| AB | CLA601 |
| AB | CLA603 |
| AB | CLA605 |
| AD | VAL154 |
| AD | ILE159 |
| AH | PHE38 |
| AH | PHE41 |
| AH | ILE45 |
| AH | LEU46 |
| AH | TYR49 |
| AH | DGD102 |
| site_id | AE1 |
| Number of Residues | 20 |
| Details | binding site for residue CLA AB 603 |
| Chain | Residue |
| AB | ARG68 |
| AB | LEU69 |
| AB | ALA146 |
| AB | LEU149 |
| AB | CYS150 |
| AB | PHE153 |
| AB | VAL198 |
| AB | HIS201 |
| AB | HIS202 |
| AB | PHE247 |
| AB | ALA248 |
| AB | VAL252 |
| AB | THR262 |
| AB | CLA602 |
| AB | CLA604 |
| AB | CLA605 |
| AB | CLA606 |
| AB | CLA609 |
| AH | PHE38 |
| AH | LEU39 |
| site_id | AE2 |
| Number of Residues | 19 |
| Details | binding site for residue CLA AB 604 |
| Chain | Residue |
| AB | TRP33 |
| AB | PHE61 |
| AB | PHE65 |
| AB | ARG68 |
| AB | LEU149 |
| AB | VAL245 |
| AB | ALA248 |
| AB | ALA249 |
| AB | VAL252 |
| AB | PHE451 |
| AB | HIS455 |
| AB | PHE458 |
| AB | ALA459 |
| AB | PHE462 |
| AB | CLA603 |
| AB | CLA605 |
| AB | CLA607 |
| AB | CLA613 |
| AB | CLA615 |
| site_id | AE3 |
| Number of Residues | 23 |
| Details | binding site for residue CLA AB 605 |
| Chain | Residue |
| AB | THR27 |
| AB | VAL30 |
| AB | ALA31 |
| AB | TRP33 |
| AB | ALA34 |
| AB | VAL62 |
| AB | PHE65 |
| AB | MET66 |
| AB | ARG68 |
| AB | LEU69 |
| AB | VAL96 |
| AB | HIS100 |
| AB | LEU103 |
| AB | GLY147 |
| AB | ALA205 |
| AB | CLA602 |
| AB | CLA603 |
| AB | CLA604 |
| AB | CLA606 |
| AB | CLA610 |
| AB | CLA612 |
| AB | CLA615 |
| AB | BCR620 |
| site_id | AE4 |
| Number of Residues | 16 |
| Details | binding site for residue CLA AB 606 |
| Chain | Residue |
| AB | LEU69 |
| AB | TRP91 |
| AB | ALA99 |
| AB | LEU103 |
| AB | LEU106 |
| AB | LEU149 |
| AB | GLY152 |
| AB | PHE153 |
| AB | PHE156 |
| AB | HIS157 |
| AB | PHE162 |
| AB | PRO164 |
| AB | CLA603 |
| AB | CLA605 |
| AB | CLA616 |
| AB | LMT624 |
| site_id | AE5 |
| Number of Residues | 17 |
| Details | binding site for residue CLA AB 607 |
| Chain | Residue |
| AB | TRP33 |
| AB | MET37 |
| AB | TYR40 |
| AB | GLN58 |
| AB | GLY59 |
| AB | PHE61 |
| AB | THR327 |
| AB | GLY328 |
| AB | PRO329 |
| AB | TRP450 |
| AB | PHE451 |
| AB | ALA454 |
| AB | CLA604 |
| AB | BCR617 |
| AB | BCR618 |
| AB | LMG622 |
| AM | PHE14 |
| site_id | AE6 |
| Number of Residues | 15 |
| Details | binding site for residue CLA AB 608 |
| Chain | Residue |
| AB | THR236 |
| AB | SER239 |
| AB | ALA243 |
| AB | PHE463 |
| AB | HIS466 |
| AB | LEU474 |
| AB | CLA609 |
| AB | CLA610 |
| AD | PHE120 |
| AD | ILE123 |
| AD | MET126 |
| AD | LEU127 |
| AD | PHE130 |
| AD | CLA404 |
| AD | SQD409 |
| site_id | AE7 |
| Number of Residues | 17 |
| Details | binding site for residue CLA AB 609 |
| Chain | Residue |
| AB | PHE139 |
| AB | VAL208 |
| AB | ALA212 |
| AB | PHE215 |
| AB | HIS216 |
| AB | PRO221 |
| AB | PRO222 |
| AB | LEU229 |
| AB | CLA603 |
| AB | CLA608 |
| AB | CLA610 |
| AH | THR27 |
| AH | THR28 |
| AH | MET31 |
| AH | PHE34 |
| AH | MET35 |
| AH | BCR101 |
| site_id | AE8 |
| Number of Residues | 11 |
| Details | binding site for residue CLA AB 610 |
| Chain | Residue |
| AB | LEU135 |
| AB | PHE139 |
| AB | HIS142 |
| AB | LEU143 |
| AB | VAL237 |
| AB | SER240 |
| AB | CLA605 |
| AB | CLA608 |
| AB | CLA609 |
| AB | CLA612 |
| AB | CLA615 |
| site_id | AE9 |
| Number of Residues | 17 |
| Details | binding site for residue CLA AB 611 |
| Chain | Residue |
| AA | LMG413 |
| AB | TRP5 |
| AB | TYR6 |
| AB | ARG7 |
| AB | VAL8 |
| AB | HIS9 |
| AB | ILE242 |
| AB | PHE462 |
| AB | PHE464 |
| AB | GLY465 |
| AB | TRP468 |
| AB | HIS469 |
| AB | ARG472 |
| AB | CLA612 |
| AB | CLA613 |
| AB | CLA614 |
| AB | LMG621 |
| site_id | AF1 |
| Number of Residues | 18 |
| Details | binding site for residue CLA AB 612 |
| Chain | Residue |
| AB | HIS9 |
| AB | LEU12 |
| AB | LEU19 |
| AB | ALA22 |
| AB | HIS23 |
| AB | HIS26 |
| AB | THR27 |
| AB | ILE234 |
| AB | VAL237 |
| AB | LEU238 |
| AB | SER241 |
| AB | VAL245 |
| AB | CLA605 |
| AB | CLA610 |
| AB | CLA611 |
| AB | CLA613 |
| AB | CLA614 |
| AB | CLA615 |
| site_id | AF2 |
| Number of Residues | 12 |
| Details | binding site for residue CLA AB 613 |
| Chain | Residue |
| AB | HIS9 |
| AB | HIS26 |
| AB | VAL30 |
| AB | LEU461 |
| AB | PHE462 |
| AB | CLA604 |
| AB | CLA611 |
| AB | CLA612 |
| AB | CLA614 |
| AB | BCR617 |
| AB | BCR619 |
| AB | LMG621 |
| site_id | AF3 |
| Number of Residues | 9 |
| Details | binding site for residue CLA AB 614 |
| Chain | Residue |
| AB | VAL8 |
| AB | HIS9 |
| AB | TRP115 |
| AB | CLA611 |
| AB | CLA612 |
| AB | CLA613 |
| AB | BCR617 |
| AL | VAL10 |
| BM | LMG102 |
| site_id | AF4 |
| Number of Residues | 12 |
| Details | binding site for residue CLA AB 615 |
| Chain | Residue |
| AB | HIS23 |
| AB | MET138 |
| AB | ILE141 |
| AB | HIS142 |
| AB | LEU145 |
| AB | CLA604 |
| AB | CLA605 |
| AB | CLA610 |
| AB | CLA612 |
| AB | CLA616 |
| AH | LEU7 |
| AH | LEU14 |
| site_id | AF5 |
| Number of Residues | 11 |
| Details | binding site for residue CLA AB 616 |
| Chain | Residue |
| AB | ILE20 |
| AB | LEU24 |
| AB | ALA110 |
| AB | TRP113 |
| AB | HIS114 |
| AB | LEU120 |
| AB | CLA606 |
| AB | CLA615 |
| AB | BCR620 |
| AH | THR5 |
| BA | SQD401 |
| site_id | AF6 |
| Number of Residues | 13 |
| Details | binding site for residue BCR AB 617 |
| Chain | Residue |
| AB | MET25 |
| AB | LEU29 |
| AB | TRP115 |
| AB | CLA607 |
| AB | CLA613 |
| AB | CLA614 |
| AB | BCR618 |
| AB | BCR619 |
| AB | LMG622 |
| AM | ILE9 |
| AM | ALA10 |
| BL | SQD101 |
| BT | PHE19 |
| site_id | AF7 |
| Number of Residues | 13 |
| Details | binding site for residue BCR AB 618 |
| Chain | Residue |
| AB | TRP33 |
| AB | SER36 |
| AB | MET37 |
| AB | CLA607 |
| AB | BCR617 |
| AB | BCR619 |
| BA | SQD401 |
| BT | ILE4 |
| BT | PHE8 |
| BT | ALA11 |
| BT | PHE17 |
| BT | PHE18 |
| BT | PHE22 |
| site_id | AF8 |
| Number of Residues | 7 |
| Details | binding site for residue BCR AB 619 |
| Chain | Residue |
| AB | LEU29 |
| AB | GLY32 |
| AB | TRP33 |
| AB | GLY105 |
| AB | CLA613 |
| AB | BCR617 |
| AB | BCR618 |
| site_id | AF9 |
| Number of Residues | 7 |
| Details | binding site for residue BCR AB 620 |
| Chain | Residue |
| AB | LEU109 |
| AB | CYS112 |
| AB | TYR117 |
| AB | CLA605 |
| AB | CLA616 |
| AB | LMT624 |
| BA | SQD401 |
| site_id | AG1 |
| Number of Residues | 10 |
| Details | binding site for residue LMG AB 621 |
| Chain | Residue |
| AA | LMG413 |
| AB | TRP5 |
| AB | TYR6 |
| AB | ARG7 |
| AB | PHE464 |
| AB | TRP468 |
| AB | CLA611 |
| AB | CLA613 |
| AD | TYR141 |
| AD | PHE269 |
| site_id | AG2 |
| Number of Residues | 10 |
| Details | binding site for residue LMG AB 622 |
| Chain | Residue |
| AB | THR327 |
| AB | GLY328 |
| AB | PRO329 |
| AB | LYS332 |
| AB | PHE453 |
| AB | CLA607 |
| AB | BCR617 |
| AL | PHE35 |
| AM | LEU6 |
| AM | LMT102 |
| site_id | AG3 |
| Number of Residues | 11 |
| Details | binding site for residue LMG AB 623 |
| Chain | Residue |
| AB | ALA43 |
| AB | TRP75 |
| AB | SER76 |
| AB | TRP78 |
| AB | LEU98 |
| BA | LEU72 |
| BA | TYR73 |
| BA | ASP103 |
| BD | ARG304 |
| BO | GLY138 |
| BT | LMT101 |
| site_id | AG4 |
| Number of Residues | 5 |
| Details | binding site for residue LMT AB 624 |
| Chain | Residue |
| AB | TRP91 |
| AB | PHE162 |
| AB | CLA606 |
| AB | BCR620 |
| AB | DGD626 |
| site_id | AG5 |
| Number of Residues | 8 |
| Details | binding site for residue LMT AB 625 |
| Chain | Residue |
| AB | ARG224 |
| AB | LEU225 |
| AB | LYS227 |
| AD | ASP16 |
| AD | ASP19 |
| AD | SQD409 |
| AH | ALA32 |
| AH | MET35 |
| site_id | AG6 |
| Number of Residues | 7 |
| Details | binding site for residue DGD AB 626 |
| Chain | Residue |
| AB | TRP75 |
| AB | ASP87 |
| AB | GLY89 |
| AB | PHE90 |
| AB | LMT624 |
| AB | LMT627 |
| BI | LMG101 |
| site_id | AG7 |
| Number of Residues | 7 |
| Details | binding site for residue LMT AB 627 |
| Chain | Residue |
| AB | GLY85 |
| AB | ASP87 |
| AB | DGD626 |
| BA | ALA100 |
| BI | MET1 |
| BI | LMG101 |
| BO | LYS95 |
| site_id | AG8 |
| Number of Residues | 15 |
| Details | binding site for residue CLA AC 501 |
| Chain | Residue |
| AC | LEU95 |
| AC | LEU168 |
| AC | GLY171 |
| AC | ALA172 |
| AC | LEU185 |
| AC | VAL233 |
| AC | HIS237 |
| AC | ILE240 |
| AC | ALA278 |
| AC | MET282 |
| AC | VAL296 |
| AC | TYR297 |
| AC | CLA502 |
| AC | CLA503 |
| AC | BCR515 |
| site_id | AG9 |
| Number of Residues | 17 |
| Details | binding site for residue CLA AC 502 |
| Chain | Residue |
| AC | TRP63 |
| AC | HIS91 |
| AC | TRP97 |
| AC | GLY171 |
| AC | LEU174 |
| AC | LYS178 |
| AC | PHE182 |
| AC | LEU279 |
| AC | MET282 |
| AC | ALA286 |
| AC | TYR297 |
| AC | HIS430 |
| AC | LEU433 |
| AC | PHE437 |
| AC | CLA501 |
| AC | CLA503 |
| AC | CLA510 |
| site_id | AH1 |
| Number of Residues | 13 |
| Details | binding site for residue CLA AC 503 |
| Chain | Residue |
| AC | ILE60 |
| AC | VAL61 |
| AC | ALA64 |
| AC | THR68 |
| AC | LEU88 |
| AC | HIS91 |
| AC | VAL114 |
| AC | HIS118 |
| AC | CLA501 |
| AC | CLA502 |
| AC | CLA510 |
| AC | CLA512 |
| AC | LMG520 |
| site_id | AH2 |
| Number of Residues | 16 |
| Details | binding site for residue CLA AC 504 |
| Chain | Residue |
| AA | PHE285 |
| AA | LHG411 |
| AC | TRP63 |
| AC | MET67 |
| AC | PHE70 |
| AC | GLN84 |
| AC | GLY85 |
| AC | ILE87 |
| AC | TRP425 |
| AC | SER429 |
| AC | CLA510 |
| AC | DGD517 |
| AC | DGD518 |
| AC | LMG519 |
| AK | PRO26 |
| AK | VAL30 |
| site_id | AH3 |
| Number of Residues | 17 |
| Details | binding site for residue CLA AC 505 |
| Chain | Residue |
| AA | PHE33 |
| AA | MET127 |
| AA | GLY128 |
| AA | TRP131 |
| AC | PHE264 |
| AC | ILE265 |
| AC | TYR274 |
| AC | GLY277 |
| AC | ALA278 |
| AC | MET281 |
| AC | HIS441 |
| AC | LEU442 |
| AC | ALA445 |
| AC | ARG449 |
| AC | CLA507 |
| AC | BCR515 |
| AI | PHE23 |
| site_id | AH4 |
| Number of Residues | 14 |
| Details | binding site for residue CLA AC 506 |
| Chain | Residue |
| AC | LEU161 |
| AC | LEU165 |
| AC | LEU213 |
| AC | ILE243 |
| AC | GLY247 |
| AC | TRP250 |
| AC | HIS251 |
| AC | THR255 |
| AC | PRO256 |
| AC | PHE257 |
| AC | TRP259 |
| AC | ALA260 |
| AC | PHE264 |
| AC | CLA507 |
| site_id | AH5 |
| Number of Residues | 13 |
| Details | binding site for residue CLA AC 507 |
| Chain | Residue |
| AC | MET157 |
| AC | LEU161 |
| AC | HIS164 |
| AC | ILE240 |
| AC | PHE264 |
| AC | TRP266 |
| AC | TYR271 |
| AC | TYR274 |
| AC | SER275 |
| AC | CLA505 |
| AC | CLA506 |
| AC | CLA509 |
| AC | BCR515 |
| site_id | AH6 |
| Number of Residues | 17 |
| Details | binding site for residue CLA AC 508 |
| Chain | Residue |
| AA | LHG411 |
| AA | SQD412 |
| AC | TRP36 |
| AC | ALA37 |
| AC | ASN39 |
| AC | ALA40 |
| AC | GLU269 |
| AC | LEU276 |
| AC | PHE436 |
| AC | PHE437 |
| AC | GLY440 |
| AC | TRP443 |
| AC | HIS444 |
| AC | ARG447 |
| AC | CLA509 |
| AC | CLA510 |
| AK | VAL30 |
| site_id | AH7 |
| Number of Residues | 17 |
| Details | binding site for residue CLA AC 509 |
| Chain | Residue |
| AC | ASN39 |
| AC | LEU42 |
| AC | ILE43 |
| AC | LEU49 |
| AC | ALA52 |
| AC | HIS53 |
| AC | TYR149 |
| AC | TRP151 |
| AC | GLY268 |
| AC | LEU272 |
| AC | SER275 |
| AC | LEU279 |
| AC | CLA507 |
| AC | CLA508 |
| AC | CLA510 |
| AC | CLA511 |
| AC | CLA512 |
| site_id | AH8 |
| Number of Residues | 17 |
| Details | binding site for residue CLA AC 510 |
| Chain | Residue |
| AA | LHG411 |
| AC | ASN39 |
| AC | HIS56 |
| AC | LEU59 |
| AC | ILE60 |
| AC | LEU279 |
| AC | PHE436 |
| AC | PHE437 |
| AC | CLA502 |
| AC | CLA503 |
| AC | CLA504 |
| AC | CLA508 |
| AC | CLA509 |
| AC | CLA511 |
| AK | PRO29 |
| AK | VAL30 |
| AK | LEU33 |
| site_id | AH9 |
| Number of Residues | 21 |
| Details | binding site for residue CLA AC 511 |
| Chain | Residue |
| AC | GLN28 |
| AC | TRP35 |
| AC | GLY38 |
| AC | ASN39 |
| AC | ARG41 |
| AC | LEU42 |
| AC | LYS48 |
| AC | ALA52 |
| AC | PHE127 |
| AC | ILE134 |
| AC | CLA509 |
| AC | CLA510 |
| AC | BCR514 |
| AK | LEU33 |
| AK | TRP39 |
| AK | GLN40 |
| AZ | VAL20 |
| AZ | PRO24 |
| Ay | ILE35 |
| Ay | ASN45 |
| Ay | LEU46 |
| site_id | AI1 |
| Number of Residues | 15 |
| Details | binding site for residue CLA AC 512 |
| Chain | Residue |
| AC | HIS53 |
| AC | ALA57 |
| AC | PHE147 |
| AC | PHE163 |
| AC | HIS164 |
| AC | VAL167 |
| AC | LEU168 |
| AC | ILE170 |
| AC | GLY171 |
| AC | LEU174 |
| AC | CLA503 |
| AC | CLA509 |
| AC | CLA513 |
| AC | LMG520 |
| AZ | BCR101 |
| site_id | AI2 |
| Number of Residues | 12 |
| Details | binding site for residue CLA AC 513 |
| Chain | Residue |
| AC | LEU50 |
| AC | VAL54 |
| AC | GLY128 |
| AC | TYR131 |
| AC | HIS132 |
| AC | PRO137 |
| AC | LEU140 |
| AC | TYR143 |
| AC | PHE147 |
| AC | ILE170 |
| AC | CLA512 |
| AZ | BCR101 |
| site_id | AI3 |
| Number of Residues | 16 |
| Details | binding site for residue BCR AC 514 |
| Chain | Residue |
| AC | ALA55 |
| AC | GLY58 |
| AC | VAL116 |
| AC | ILE120 |
| AC | SER122 |
| AC | ALA123 |
| AC | CLA511 |
| AK | TYR15 |
| AK | PHE18 |
| AK | PHE32 |
| AK | TRP39 |
| AK | BCR102 |
| AZ | LEU9 |
| AZ | VAL13 |
| AZ | VAL20 |
| AZ | BCR101 |
| site_id | AI4 |
| Number of Residues | 15 |
| Details | binding site for residue BCR AC 515 |
| Chain | Residue |
| AC | ILE209 |
| AC | PHE210 |
| AC | TYR212 |
| AC | LEU213 |
| AC | ASP232 |
| AC | VAL233 |
| AC | HIS237 |
| AC | ILE240 |
| AC | PHE264 |
| AC | CLA501 |
| AC | CLA505 |
| AC | CLA507 |
| AI | VAL20 |
| AI | PHE23 |
| AI | LEU24 |
| site_id | AI5 |
| Number of Residues | 19 |
| Details | binding site for residue DGD AC 516 |
| Chain | Residue |
| AA | LEU151 |
| AA | PHE155 |
| AA | ILE163 |
| AC | PRO217 |
| AC | PHE218 |
| AC | GLY219 |
| AC | GLY220 |
| AC | GLY222 |
| AC | VAL225 |
| AC | SER226 |
| AC | PHE284 |
| AC | CYS288 |
| AC | PHE292 |
| AC | ASN294 |
| AC | THR305 |
| AC | PRO307 |
| AC | PHE361 |
| AC | ARG362 |
| AC | LEU438 |
| site_id | AI6 |
| Number of Residues | 18 |
| Details | binding site for residue DGD AC 517 |
| Chain | Residue |
| AA | PHE197 |
| AC | TYR82 |
| AC | GLU83 |
| AC | GLN84 |
| AC | GLY85 |
| AC | LEU404 |
| AC | SER406 |
| AC | ASN418 |
| AC | VAL420 |
| AC | TRP425 |
| AC | THR428 |
| AC | SER429 |
| AC | CLA504 |
| AC | DGD518 |
| AC | LMG519 |
| AC | LHG521 |
| AJ | TYR33 |
| AJ | BCR102 |
| site_id | AI7 |
| Number of Residues | 20 |
| Details | binding site for residue DGD AC 518 |
| Chain | Residue |
| AA | LEU200 |
| AA | TRP278 |
| AA | PHE300 |
| AA | PHE302 |
| AA | SER305 |
| AA | SQD412 |
| AC | ASN405 |
| AC | ASN415 |
| AC | SER416 |
| AC | ASN418 |
| AC | CLA504 |
| AC | DGD517 |
| AJ | PHE29 |
| AJ | ALA32 |
| AJ | TYR33 |
| AJ | GLY37 |
| AJ | SER38 |
| AJ | SER39 |
| AJ | BCR102 |
| AV | GLN60 |
| site_id | AI8 |
| Number of Residues | 7 |
| Details | binding site for residue LMG AC 519 |
| Chain | Residue |
| AC | HIS74 |
| AC | CLA504 |
| AC | DGD517 |
| AJ | BCR102 |
| AK | ASP23 |
| AK | VAL30 |
| Ay | ILE25 |
| site_id | AI9 |
| Number of Residues | 10 |
| Details | binding site for residue LMG AC 520 |
| Chain | Residue |
| AC | TRP97 |
| AC | ASP107 |
| AC | PHE109 |
| AC | VAL113 |
| AC | VAL114 |
| AC | VAL117 |
| AC | HIS118 |
| AC | CLA503 |
| AC | CLA512 |
| AZ | PHE59 |
| site_id | AJ1 |
| Number of Residues | 8 |
| Details | binding site for residue LHG AC 521 |
| Chain | Residue |
| AA | TYR262 |
| AA | ASN266 |
| AA | SQD412 |
| AC | TRP35 |
| AC | DGD517 |
| AE | LMG102 |
| AJ | BCR102 |
| AK | PHE45 |
| site_id | AJ2 |
| Number of Residues | 8 |
| Details | binding site for residue BCT AD 401 |
| Chain | Residue |
| AA | HIS215 |
| AA | TYR246 |
| AA | HIS272 |
| AA | FE2401 |
| AD | HIS214 |
| AD | TYR244 |
| AD | LYS264 |
| AD | HIS268 |
| site_id | AJ3 |
| Number of Residues | 23 |
| Details | binding site for residue CLA AD 402 |
| Chain | Residue |
| AA | PHE206 |
| AA | CLA402 |
| AA | CLA403 |
| AA | CLA404 |
| AD | TRP48 |
| AD | PRO149 |
| AD | VAL152 |
| AD | PHE153 |
| AD | VAL156 |
| AD | PHE181 |
| AD | LEU182 |
| AD | PHE185 |
| AD | GLN186 |
| AD | TRP191 |
| AD | THR192 |
| AD | HIS197 |
| AD | GLY200 |
| AD | VAL201 |
| AD | VAL204 |
| AD | LEU279 |
| AD | SER282 |
| AD | ALA283 |
| AD | PHO403 |
| site_id | AJ4 |
| Number of Residues | 19 |
| Details | binding site for residue PHO AD 403 |
| Chain | Residue |
| AA | PHE206 |
| AA | LEU210 |
| AA | MET214 |
| AA | CLA404 |
| AD | LEU37 |
| AD | ALA41 |
| AD | TRP48 |
| AD | GLY118 |
| AD | LEU122 |
| AD | PHE125 |
| AD | ASN142 |
| AD | ALA145 |
| AD | PHE146 |
| AD | ALA148 |
| AD | PRO149 |
| AD | PHE153 |
| AD | PRO275 |
| AD | LEU279 |
| AD | CLA402 |
| site_id | AJ5 |
| Number of Residues | 15 |
| Details | binding site for residue CLA AD 404 |
| Chain | Residue |
| AB | CLA608 |
| AD | LEU43 |
| AD | LEU89 |
| AD | LEU90 |
| AD | LEU91 |
| AD | LEU92 |
| AD | TRP93 |
| AD | TRP104 |
| AD | THR112 |
| AD | PHE113 |
| AD | HIS117 |
| AD | LMT411 |
| AX | GLY22 |
| AX | LEU23 |
| AX | GLY26 |
| site_id | AJ6 |
| Number of Residues | 18 |
| Details | binding site for residue PL9 AD 405 |
| Chain | Residue |
| AA | PHE52 |
| AA | ILE53 |
| AA | ILE77 |
| AA | CLA403 |
| AD | MET199 |
| AD | ALA202 |
| AD | HIS214 |
| AD | THR217 |
| AD | TRP253 |
| AD | ALA260 |
| AD | PHE261 |
| AD | LEU267 |
| AD | PHE273 |
| AD | VAL274 |
| AD | THR277 |
| AL | LEU23 |
| AL | VAL26 |
| AL | LEU29 |
| site_id | AJ7 |
| Number of Residues | 11 |
| Details | binding site for residue BCR AD 406 |
| Chain | Residue |
| AD | TYR42 |
| AD | GLY46 |
| AD | GLY47 |
| AD | LEU49 |
| AD | THR50 |
| AD | PHE101 |
| AF | PRO29 |
| AF | PHE33 |
| AJ | VAL21 |
| AJ | VAL25 |
| AJ | PL9101 |
| site_id | AJ8 |
| Number of Residues | 12 |
| Details | binding site for residue LMG AD 407 |
| Chain | Residue |
| AA | CLA404 |
| AD | TYR67 |
| AD | GLY70 |
| AD | CYS71 |
| AD | PHE73 |
| AF | ILE37 |
| AF | MET40 |
| AF | GLN41 |
| AJ | PHE28 |
| AJ | GLY31 |
| AJ | ALA32 |
| AJ | GLY37 |
| site_id | AJ9 |
| Number of Residues | 12 |
| Details | binding site for residue LMG AD 408 |
| Chain | Residue |
| AD | PHE257 |
| AD | ALA260 |
| AD | PHE261 |
| AD | SER262 |
| AD | ASN263 |
| AD | TRP266 |
| AD | PHE270 |
| AL | THR15 |
| AL | TYR18 |
| AL | LEU19 |
| AT | PHE17 |
| AT | ALA20 |
| site_id | AK1 |
| Number of Residues | 10 |
| Details | binding site for residue SQD AD 409 |
| Chain | Residue |
| AB | LYS227 |
| AB | ALA228 |
| AB | ARG230 |
| AB | LEU474 |
| AB | CLA608 |
| AB | LMT625 |
| AD | LYS23 |
| AD | TRP32 |
| AD | ARG134 |
| AD | LEU135 |
| site_id | AK2 |
| Number of Residues | 6 |
| Details | binding site for residue DGD AD 410 |
| Chain | Residue |
| AD | ASP100 |
| AD | PHE101 |
| AD | LMT411 |
| AE | LEU42 |
| AE | ASP45 |
| AE | VAL46 |
| site_id | AK3 |
| Number of Residues | 8 |
| Details | binding site for residue LMT AD 411 |
| Chain | Residue |
| AD | LEU92 |
| AD | TRP93 |
| AD | GLY99 |
| AD | CLA404 |
| AD | DGD410 |
| AX | ILE21 |
| AX | SER25 |
| AX | GLY26 |
| site_id | AK4 |
| Number of Residues | 14 |
| Details | binding site for residue HEM AE 101 |
| Chain | Residue |
| AE | ARG8 |
| AE | ILE13 |
| AE | ARG18 |
| AE | TYR19 |
| AE | HIS23 |
| AE | THR26 |
| AE | ILE27 |
| AE | LEU30 |
| AF | ILE15 |
| AF | ARG19 |
| AF | TRP20 |
| AF | HIS24 |
| AF | ALA27 |
| AF | ILE31 |
| site_id | AK5 |
| Number of Residues | 7 |
| Details | binding site for residue LMG AE 102 |
| Chain | Residue |
| AA | TYR262 |
| AC | LHG521 |
| AD | PHE27 |
| AE | PRO9 |
| AE | PHE10 |
| AE | SER11 |
| AJ | PL9101 |
| site_id | AK6 |
| Number of Residues | 9 |
| Details | binding site for residue SQD AF 101 |
| Chain | Residue |
| AD | TRP21 |
| AD | ARG24 |
| AD | ARG26 |
| AE | GLU7 |
| AF | PHE16 |
| AF | THR17 |
| AF | VAL18 |
| AX | THR33 |
| AX | ILE40 |
| site_id | AK7 |
| Number of Residues | 8 |
| Details | binding site for residue BCR AH 101 |
| Chain | Residue |
| AB | CLA601 |
| AB | CLA609 |
| AH | MET35 |
| AH | PHE38 |
| AH | PHE41 |
| AX | THR11 |
| AX | ILE12 |
| AX | LEU16 |
| site_id | AK8 |
| Number of Residues | 14 |
| Details | binding site for residue DGD AH 102 |
| Chain | Residue |
| AB | TYR193 |
| AB | PHE250 |
| AB | TYR258 |
| AB | TYR273 |
| AB | SER277 |
| AB | PHE463 |
| AB | CLA602 |
| AD | HIS87 |
| AD | LEU116 |
| AD | SER165 |
| AH | TYR49 |
| AH | VAL60 |
| AH | SER61 |
| AH | TRP62 |
| site_id | AK9 |
| Number of Residues | 6 |
| Details | binding site for residue LMG AI 101 |
| Chain | Residue |
| AI | MET1 |
| AI | THR3 |
| AI | LEU4 |
| AI | LMT102 |
| BB | DGD602 |
| BB | LMT603 |
| site_id | AL1 |
| Number of Residues | 5 |
| Details | binding site for residue LMT AI 102 |
| Chain | Residue |
| AI | THR3 |
| AI | ILE6 |
| AI | ILE10 |
| AI | VAL11 |
| AI | LMG101 |
| site_id | AL2 |
| Number of Residues | 6 |
| Details | binding site for residue PL9 AJ 101 |
| Chain | Residue |
| AA | PL9407 |
| AA | SQD412 |
| AD | BCR406 |
| AE | LMG102 |
| AJ | VAL16 |
| AJ | GLY20 |
| site_id | AL3 |
| Number of Residues | 7 |
| Details | binding site for residue BCR AJ 102 |
| Chain | Residue |
| AC | DGD517 |
| AC | DGD518 |
| AC | LMG519 |
| AC | LHG521 |
| AJ | PHE29 |
| AJ | TYR33 |
| AK | BCR102 |
| site_id | AL4 |
| Number of Residues | 2 |
| Details | binding site for residue CA AK 101 |
| Chain | Residue |
| AK | ASP19 |
| AK | ASP23 |
| site_id | AL5 |
| Number of Residues | 17 |
| Details | binding site for residue BCR AK 102 |
| Chain | Residue |
| AC | BCR514 |
| AJ | ALA14 |
| AJ | THR15 |
| AJ | GLY18 |
| AJ | MET19 |
| AJ | BCR102 |
| AK | LEU21 |
| AK | LEU25 |
| AK | LEU31 |
| AK | PHE32 |
| AK | PHE37 |
| AK | VAL38 |
| AZ | VAL13 |
| AZ | SER16 |
| Ay | ILE28 |
| Ay | GLY29 |
| Ay | GLY32 |
| site_id | AL6 |
| Number of Residues | 8 |
| Details | binding site for residue LMG AM 101 |
| Chain | Residue |
| AM | ILE23 |
| AM | GLU30 |
| AM | SER31 |
| AM | GLN33 |
| BB | CLA617 |
| BL | VAL10 |
| BM | ILE24 |
| BM | GLN32 |
| site_id | AL7 |
| Number of Residues | 4 |
| Details | binding site for residue LMT AM 102 |
| Chain | Residue |
| AB | TYR40 |
| AB | LMG622 |
| AM | GLN5 |
| BM | MET1 |
| site_id | AL8 |
| Number of Residues | 3 |
| Details | binding site for residue CA AO 301 |
| Chain | Residue |
| AO | GLU81 |
| AO | GLU140 |
| AO | HIS257 |
| site_id | AL9 |
| Number of Residues | 6 |
| Details | binding site for residue LMT AT 101 |
| Chain | Residue |
| AA | LEU72 |
| AA | LMG416 |
| AT | VAL7 |
| BB | SER36 |
| BB | ALA43 |
| BB | THR44 |
| site_id | AM1 |
| Number of Residues | 13 |
| Details | binding site for residue BCR AT 102 |
| Chain | Residue |
| AA | SQD415 |
| AT | ILE4 |
| AT | PHE8 |
| AT | ALA11 |
| AT | PHE17 |
| AT | PHE18 |
| AT | PHE22 |
| BB | TRP33 |
| BB | SER36 |
| BB | MET37 |
| BB | CLA610 |
| BB | BCR620 |
| BB | BCR621 |
| site_id | AM2 |
| Number of Residues | 14 |
| Details | binding site for residue HEM AV 201 |
| Chain | Residue |
| AV | ALA62 |
| AV | CYS63 |
| AV | CYS66 |
| AV | HIS67 |
| AV | THR74 |
| AV | LEU78 |
| AV | ASP79 |
| AV | THR84 |
| AV | ALA88 |
| AV | LEU98 |
| AV | TYR101 |
| AV | MET102 |
| AV | TYR108 |
| AV | HIS118 |
| site_id | AM3 |
| Number of Residues | 11 |
| Details | binding site for residue BCR AZ 101 |
| Chain | Residue |
| AC | PHE112 |
| AC | VAL116 |
| AC | VAL124 |
| AC | LEU125 |
| AC | CLA512 |
| AC | CLA513 |
| AC | BCR514 |
| AK | TYR15 |
| AZ | VAL54 |
| AZ | GLY55 |
| AZ | ASN58 |
| site_id | AM4 |
| Number of Residues | 10 |
| Details | binding site for residue SQD BA 401 |
| Chain | Residue |
| AB | TRP113 |
| AB | TYR117 |
| AB | CLA616 |
| AB | BCR618 |
| AB | BCR620 |
| BA | TRP20 |
| BA | ASN26 |
| BA | ARG27 |
| BA | LEU28 |
| BA | LEU42 |
| site_id | AM5 |
| Number of Residues | 5 |
| Details | binding site for residue FE2 BA 402 |
| Chain | Residue |
| BA | HIS215 |
| BA | HIS272 |
| BD | HIS214 |
| BD | HIS268 |
| BD | BCT401 |
| site_id | AM6 |
| Number of Residues | 20 |
| Details | binding site for residue CLA BA 403 |
| Chain | Residue |
| BA | PHE119 |
| BA | TYR147 |
| BA | SER153 |
| BA | ALA154 |
| BA | VAL157 |
| BA | MET183 |
| BA | PHE186 |
| BA | GLN187 |
| BA | LEU193 |
| BA | HIS198 |
| BA | GLY201 |
| BA | VAL205 |
| BA | THR286 |
| BA | ILE290 |
| BA | CLA404 |
| BA | CLA405 |
| BA | PHO406 |
| BD | LEU182 |
| BD | CLA402 |
| BT | PHE17 |
| site_id | AM7 |
| Number of Residues | 17 |
| Details | binding site for residue CLA BA 404 |
| Chain | Residue |
| BA | THR45 |
| BA | VAL157 |
| BA | PHE158 |
| BA | MET172 |
| BA | ILE176 |
| BA | THR179 |
| BA | MET183 |
| BA | CLA403 |
| BA | PHO406 |
| BA | LMG414 |
| BD | MET198 |
| BD | VAL201 |
| BD | ALA202 |
| BD | GLY206 |
| BD | CLA402 |
| BD | PL9405 |
| BL | LEU30 |
| site_id | AM8 |
| Number of Residues | 14 |
| Details | binding site for residue CLA BA 405 |
| Chain | Residue |
| BA | GLN199 |
| BA | VAL202 |
| BA | ALA203 |
| BA | GLY207 |
| BA | TRP278 |
| BA | CLA403 |
| BD | PHE157 |
| BD | VAL175 |
| BD | ILE178 |
| BD | PHE179 |
| BD | LEU182 |
| BD | CLA402 |
| BD | PHO403 |
| BD | LMG407 |
| site_id | AM9 |
| Number of Residues | 20 |
| Details | binding site for residue PHO BA 406 |
| Chain | Residue |
| BA | LEU41 |
| BA | ALA44 |
| BA | THR45 |
| BA | ILE115 |
| BA | TYR126 |
| BA | GLN130 |
| BA | ALA146 |
| BA | TYR147 |
| BA | PRO150 |
| BA | LEU174 |
| BA | GLY175 |
| BA | VAL283 |
| BA | CLA403 |
| BA | CLA404 |
| BD | LEU205 |
| BD | ALA208 |
| BD | LEU209 |
| BD | ILE213 |
| BD | TRP253 |
| BD | PHE257 |
| site_id | AN1 |
| Number of Residues | 14 |
| Details | binding site for residue CLA BA 407 |
| Chain | Residue |
| BA | ILE36 |
| BA | PRO39 |
| BA | THR40 |
| BA | PHE93 |
| BA | PRO95 |
| BA | ILE96 |
| BA | TRP97 |
| BA | LEU114 |
| BA | PHE117 |
| BA | HIS118 |
| BA | LEU121 |
| BA | DGD411 |
| BI | TYR9 |
| BI | VAL12 |
| site_id | AN2 |
| Number of Residues | 17 |
| Details | binding site for residue PL9 BA 408 |
| Chain | Residue |
| BA | PHE211 |
| BA | MET214 |
| BA | HIS215 |
| BA | LEU218 |
| BA | HIS252 |
| BA | PHE255 |
| BA | SER264 |
| BA | PHE265 |
| BA | LEU271 |
| BA | PHE274 |
| BD | PHE38 |
| BD | ALA41 |
| BD | TYR42 |
| BD | LEU45 |
| BF | ALA22 |
| BF | THR25 |
| BJ | PL9101 |
| site_id | AN3 |
| Number of Residues | 7 |
| Details | binding site for residue OEC BA 409 |
| Chain | Residue |
| BA | ASP170 |
| BA | GLU189 |
| BA | HIS332 |
| BA | GLU333 |
| BA | ASP342 |
| BA | ALA344 |
| BC | GLU354 |
| site_id | AN4 |
| Number of Residues | 7 |
| Details | binding site for residue BCR BA 410 |
| Chain | Residue |
| BA | ILE38 |
| BA | LEU42 |
| BA | ALA43 |
| BA | CYS47 |
| BA | ALA51 |
| BA | TRP105 |
| BI | PHE15 |
| site_id | AN5 |
| Number of Residues | 15 |
| Details | binding site for residue DGD BA 411 |
| Chain | Residue |
| BA | PHE93 |
| BA | PRO95 |
| BA | TRP97 |
| BA | GLU98 |
| BA | CLA407 |
| BC | LEU214 |
| BC | LYS215 |
| BC | SER216 |
| BC | PRO217 |
| BC | PHE218 |
| BC | TRP223 |
| BC | PHE284 |
| BI | LYS5 |
| BI | TYR9 |
| BO | GLY38 |
| site_id | AN6 |
| Number of Residues | 15 |
| Details | binding site for residue LHG BA 412 |
| Chain | Residue |
| BA | ARG140 |
| BA | TRP142 |
| BA | PHE273 |
| BA | SQD413 |
| BC | TRP36 |
| BC | TRP443 |
| BC | ARG447 |
| BC | CLA504 |
| BC | CLA508 |
| BD | GLU219 |
| BD | ASN220 |
| BD | ALA229 |
| BD | SER230 |
| BD | THR231 |
| BD | PHE232 |
| site_id | AN7 |
| Number of Residues | 11 |
| Details | binding site for residue SQD BA 413 |
| Chain | Residue |
| BA | ASN267 |
| BA | SER270 |
| BA | PHE273 |
| BA | LHG412 |
| BC | TRP36 |
| BC | DGD518 |
| BC | LHG521 |
| BD | PHE232 |
| BD | ARG233 |
| BJ | PL9101 |
| BK | PHE37 |
| site_id | AN8 |
| Number of Residues | 17 |
| Details | binding site for residue LMG BA 414 |
| Chain | Residue |
| BA | SER232 |
| BA | ASN234 |
| BA | CLA404 |
| BB | TRP5 |
| BB | TYR6 |
| BB | CLA614 |
| BB | LMG623 |
| BD | TRP266 |
| BD | PHE273 |
| BL | GLU11 |
| BL | LEU12 |
| BL | ASN13 |
| BL | SER16 |
| BL | LEU19 |
| BL | GLY20 |
| BL | LEU22 |
| BL | VAL26 |
| site_id | AN9 |
| Number of Residues | 3 |
| Details | binding site for residue CL BA 415 |
| Chain | Residue |
| BA | HIS332 |
| BA | GLU333 |
| BD | LYS317 |
| site_id | AO1 |
| Number of Residues | 10 |
| Details | binding site for residue SQD BB 601 |
| Chain | Residue |
| AL | ARG14 |
| AL | TYR18 |
| AM | TYR26 |
| AT | PHE23 |
| BB | ARG18 |
| BB | LEU29 |
| BB | SER104 |
| BB | CLA617 |
| BB | BCR620 |
| BL | ASN4 |
| site_id | AO2 |
| Number of Residues | 8 |
| Details | binding site for residue DGD BB 602 |
| Chain | Residue |
| AI | LMG101 |
| BB | TRP75 |
| BB | ASP87 |
| BB | GLY89 |
| BB | PHE90 |
| BB | TRP91 |
| BB | LMT603 |
| BB | LMT625 |
| site_id | AO3 |
| Number of Residues | 7 |
| Details | binding site for residue LMT BB 603 |
| Chain | Residue |
| AA | ALA100 |
| AI | MET1 |
| AI | LMG101 |
| AO | LYS95 |
| BB | GLY85 |
| BB | ASP87 |
| BB | DGD602 |
| site_id | AO4 |
| Number of Residues | 10 |
| Details | binding site for residue CLA BB 604 |
| Chain | Residue |
| BB | TRP185 |
| BB | PRO187 |
| BB | PHE190 |
| BB | ILE207 |
| BB | VAL208 |
| BB | CLA605 |
| BH | PHE41 |
| BH | ILE44 |
| BO | THR51 |
| BX | BCR101 |
| site_id | AO5 |
| Number of Residues | 20 |
| Details | binding site for residue CLA BB 605 |
| Chain | Residue |
| BB | GLU184 |
| BB | GLY189 |
| BB | PHE190 |
| BB | GLY197 |
| BB | ALA200 |
| BB | HIS201 |
| BB | ALA205 |
| BB | VAL208 |
| BB | PHE246 |
| BB | PHE247 |
| BB | CLA604 |
| BB | CLA606 |
| BD | VAL154 |
| BD | ILE159 |
| BH | PHE38 |
| BH | PHE41 |
| BH | ILE45 |
| BH | LEU46 |
| BH | TYR49 |
| BH | DGD101 |
| site_id | AO6 |
| Number of Residues | 20 |
| Details | binding site for residue CLA BB 606 |
| Chain | Residue |
| BB | ARG68 |
| BB | LEU69 |
| BB | ALA146 |
| BB | LEU149 |
| BB | CYS150 |
| BB | PHE153 |
| BB | VAL198 |
| BB | HIS201 |
| BB | HIS202 |
| BB | PHE247 |
| BB | ALA248 |
| BB | VAL252 |
| BB | THR262 |
| BB | CLA605 |
| BB | CLA607 |
| BB | CLA608 |
| BB | CLA609 |
| BB | CLA612 |
| BH | PHE38 |
| BH | LEU39 |
| site_id | AO7 |
| Number of Residues | 19 |
| Details | binding site for residue CLA BB 607 |
| Chain | Residue |
| BB | TRP33 |
| BB | PHE61 |
| BB | PHE65 |
| BB | ARG68 |
| BB | LEU149 |
| BB | VAL245 |
| BB | ALA248 |
| BB | ALA249 |
| BB | VAL252 |
| BB | PHE451 |
| BB | HIS455 |
| BB | PHE458 |
| BB | ALA459 |
| BB | PHE462 |
| BB | CLA606 |
| BB | CLA608 |
| BB | CLA610 |
| BB | CLA616 |
| BB | CLA618 |
| site_id | AO8 |
| Number of Residues | 20 |
| Details | binding site for residue CLA BB 608 |
| Chain | Residue |
| BB | THR27 |
| BB | VAL30 |
| BB | ALA31 |
| BB | TRP33 |
| BB | ALA34 |
| BB | VAL62 |
| BB | PHE65 |
| BB | MET66 |
| BB | ARG68 |
| BB | LEU69 |
| BB | HIS100 |
| BB | LEU103 |
| BB | GLY147 |
| BB | ALA205 |
| BB | CLA606 |
| BB | CLA607 |
| BB | CLA609 |
| BB | CLA613 |
| BB | CLA615 |
| BB | BCR622 |
| site_id | AO9 |
| Number of Residues | 16 |
| Details | binding site for residue CLA BB 609 |
| Chain | Residue |
| BB | LEU69 |
| BB | TRP91 |
| BB | ALA99 |
| BB | LEU103 |
| BB | LEU106 |
| BB | LEU149 |
| BB | GLY152 |
| BB | PHE153 |
| BB | PHE156 |
| BB | HIS157 |
| BB | PHE162 |
| BB | PRO164 |
| BB | CLA606 |
| BB | CLA608 |
| BB | CLA619 |
| BB | LMT625 |
| site_id | AP1 |
| Number of Residues | 17 |
| Details | binding site for residue CLA BB 610 |
| Chain | Residue |
| AT | BCR102 |
| BB | TRP33 |
| BB | MET37 |
| BB | TYR40 |
| BB | GLN58 |
| BB | GLY59 |
| BB | PHE61 |
| BB | THR327 |
| BB | GLY328 |
| BB | PRO329 |
| BB | TRP450 |
| BB | PHE451 |
| BB | ALA454 |
| BB | CLA607 |
| BB | BCR620 |
| BB | LMG624 |
| BM | PHE14 |
| site_id | AP2 |
| Number of Residues | 15 |
| Details | binding site for residue CLA BB 611 |
| Chain | Residue |
| BB | THR236 |
| BB | SER239 |
| BB | ALA243 |
| BB | PHE463 |
| BB | HIS466 |
| BB | LEU474 |
| BB | CLA612 |
| BB | CLA613 |
| BD | PHE120 |
| BD | ILE123 |
| BD | MET126 |
| BD | LEU127 |
| BD | PHE130 |
| BD | CLA404 |
| BH | LEU43 |
| site_id | AP3 |
| Number of Residues | 17 |
| Details | binding site for residue CLA BB 612 |
| Chain | Residue |
| BB | PHE139 |
| BB | VAL208 |
| BB | ALA212 |
| BB | PHE215 |
| BB | HIS216 |
| BB | PRO221 |
| BB | PRO222 |
| BB | LEU229 |
| BB | CLA606 |
| BB | CLA611 |
| BB | CLA613 |
| BH | THR27 |
| BH | THR28 |
| BH | MET31 |
| BH | PHE34 |
| BH | MET35 |
| BX | BCR101 |
| site_id | AP4 |
| Number of Residues | 11 |
| Details | binding site for residue CLA BB 613 |
| Chain | Residue |
| BB | LEU135 |
| BB | PHE139 |
| BB | HIS142 |
| BB | LEU143 |
| BB | VAL237 |
| BB | SER240 |
| BB | CLA608 |
| BB | CLA611 |
| BB | CLA612 |
| BB | CLA615 |
| BB | CLA618 |
| site_id | AP5 |
| Number of Residues | 17 |
| Details | binding site for residue CLA BB 614 |
| Chain | Residue |
| BA | LMG414 |
| BB | TRP5 |
| BB | TYR6 |
| BB | ARG7 |
| BB | VAL8 |
| BB | HIS9 |
| BB | ILE242 |
| BB | PHE462 |
| BB | PHE464 |
| BB | GLY465 |
| BB | TRP468 |
| BB | HIS469 |
| BB | ARG472 |
| BB | CLA615 |
| BB | CLA616 |
| BB | CLA617 |
| BB | LMG623 |
| site_id | AP6 |
| Number of Residues | 16 |
| Details | binding site for residue CLA BB 615 |
| Chain | Residue |
| BB | HIS9 |
| BB | LEU12 |
| BB | LEU19 |
| BB | ALA22 |
| BB | HIS23 |
| BB | HIS26 |
| BB | THR27 |
| BB | VAL237 |
| BB | LEU238 |
| BB | SER241 |
| BB | CLA608 |
| BB | CLA613 |
| BB | CLA614 |
| BB | CLA616 |
| BB | CLA617 |
| BB | CLA618 |
| site_id | AP7 |
| Number of Residues | 12 |
| Details | binding site for residue CLA BB 616 |
| Chain | Residue |
| BB | HIS9 |
| BB | HIS26 |
| BB | VAL30 |
| BB | LEU461 |
| BB | PHE462 |
| BB | CLA607 |
| BB | CLA614 |
| BB | CLA615 |
| BB | CLA617 |
| BB | BCR620 |
| BB | BCR621 |
| BB | LMG623 |
| site_id | AP8 |
| Number of Residues | 10 |
| Details | binding site for residue CLA BB 617 |
| Chain | Residue |
| AM | LMG101 |
| BB | VAL8 |
| BB | HIS9 |
| BB | TRP115 |
| BB | SQD601 |
| BB | CLA614 |
| BB | CLA615 |
| BB | CLA616 |
| BB | BCR620 |
| BL | VAL10 |
| site_id | AP9 |
| Number of Residues | 10 |
| Details | binding site for residue CLA BB 618 |
| Chain | Residue |
| BB | HIS23 |
| BB | MET138 |
| BB | ILE141 |
| BB | HIS142 |
| BB | LEU145 |
| BB | CLA607 |
| BB | CLA613 |
| BB | CLA615 |
| BB | CLA619 |
| BH | LEU14 |
| site_id | AQ1 |
| Number of Residues | 11 |
| Details | binding site for residue CLA BB 619 |
| Chain | Residue |
| AA | SQD415 |
| BB | ILE20 |
| BB | LEU24 |
| BB | ALA110 |
| BB | TRP113 |
| BB | HIS114 |
| BB | LEU120 |
| BB | CLA609 |
| BB | CLA618 |
| BB | BCR622 |
| BH | THR5 |
| site_id | AQ2 |
| Number of Residues | 13 |
| Details | binding site for residue BCR BB 620 |
| Chain | Residue |
| AT | PHE19 |
| AT | BCR102 |
| BB | MET25 |
| BB | LEU29 |
| BB | TRP115 |
| BB | SQD601 |
| BB | CLA610 |
| BB | CLA616 |
| BB | CLA617 |
| BB | BCR621 |
| BB | LMG624 |
| BM | ILE9 |
| BM | ALA10 |
| site_id | AQ3 |
| Number of Residues | 7 |
| Details | binding site for residue BCR BB 621 |
| Chain | Residue |
| AT | BCR102 |
| BB | LEU29 |
| BB | GLY32 |
| BB | TRP33 |
| BB | GLY105 |
| BB | CLA616 |
| BB | BCR620 |
| site_id | AQ4 |
| Number of Residues | 9 |
| Details | binding site for residue BCR BB 622 |
| Chain | Residue |
| AA | SQD415 |
| AT | PHE22 |
| AT | PHE23 |
| BB | LEU109 |
| BB | CYS112 |
| BB | TYR117 |
| BB | CLA608 |
| BB | CLA619 |
| BB | LMT625 |
| site_id | AQ5 |
| Number of Residues | 10 |
| Details | binding site for residue LMG BB 623 |
| Chain | Residue |
| BA | LMG414 |
| BB | TRP5 |
| BB | TYR6 |
| BB | ARG7 |
| BB | PHE464 |
| BB | TRP468 |
| BB | CLA614 |
| BB | CLA616 |
| BD | TYR141 |
| BD | PHE269 |
| site_id | AQ6 |
| Number of Residues | 10 |
| Details | binding site for residue LMG BB 624 |
| Chain | Residue |
| BB | THR327 |
| BB | GLY328 |
| BB | PRO329 |
| BB | LYS332 |
| BB | PHE453 |
| BB | CLA610 |
| BB | BCR620 |
| BL | PHE35 |
| BM | LEU6 |
| BM | LMT101 |
| site_id | AQ7 |
| Number of Residues | 5 |
| Details | binding site for residue LMT BB 625 |
| Chain | Residue |
| BB | TRP91 |
| BB | PHE162 |
| BB | DGD602 |
| BB | CLA609 |
| BB | BCR622 |
| site_id | AQ8 |
| Number of Residues | 8 |
| Details | binding site for residue LMT BB 626 |
| Chain | Residue |
| BB | ARG224 |
| BB | LEU225 |
| BB | LYS227 |
| BD | ASP16 |
| BD | ASP19 |
| BD | SQD409 |
| BH | ALA32 |
| BH | MET35 |
| site_id | AQ9 |
| Number of Residues | 15 |
| Details | binding site for residue CLA BC 501 |
| Chain | Residue |
| BC | LEU95 |
| BC | LEU168 |
| BC | GLY171 |
| BC | ALA172 |
| BC | LEU185 |
| BC | VAL233 |
| BC | HIS237 |
| BC | ILE240 |
| BC | ALA278 |
| BC | MET282 |
| BC | VAL296 |
| BC | TYR297 |
| BC | CLA502 |
| BC | CLA503 |
| BC | BCR515 |
| site_id | AR1 |
| Number of Residues | 17 |
| Details | binding site for residue CLA BC 502 |
| Chain | Residue |
| BC | TRP63 |
| BC | HIS91 |
| BC | LEU95 |
| BC | TRP97 |
| BC | GLY171 |
| BC | LEU174 |
| BC | LYS178 |
| BC | LEU279 |
| BC | MET282 |
| BC | ALA286 |
| BC | TYR297 |
| BC | HIS430 |
| BC | LEU433 |
| BC | PHE437 |
| BC | CLA501 |
| BC | CLA503 |
| BC | CLA510 |
| site_id | AR2 |
| Number of Residues | 14 |
| Details | binding site for residue CLA BC 503 |
| Chain | Residue |
| BC | ILE60 |
| BC | VAL61 |
| BC | ALA64 |
| BC | THR68 |
| BC | LEU88 |
| BC | HIS91 |
| BC | VAL114 |
| BC | HIS118 |
| BC | MET282 |
| BC | CLA501 |
| BC | CLA502 |
| BC | CLA510 |
| BC | CLA512 |
| BC | LMG520 |
| site_id | AR3 |
| Number of Residues | 16 |
| Details | binding site for residue CLA BC 504 |
| Chain | Residue |
| BA | PHE285 |
| BA | LHG412 |
| BC | TRP63 |
| BC | MET67 |
| BC | PHE70 |
| BC | GLN84 |
| BC | GLY85 |
| BC | ILE87 |
| BC | TRP425 |
| BC | SER429 |
| BC | CLA510 |
| BC | DGD517 |
| BC | DGD518 |
| BC | LMG519 |
| BK | PRO26 |
| BK | VAL30 |
| site_id | AR4 |
| Number of Residues | 17 |
| Details | binding site for residue CLA BC 505 |
| Chain | Residue |
| BA | PHE33 |
| BA | MET127 |
| BA | GLY128 |
| BA | TRP131 |
| BC | PHE264 |
| BC | ILE265 |
| BC | TYR274 |
| BC | GLY277 |
| BC | ALA278 |
| BC | MET281 |
| BC | HIS441 |
| BC | LEU442 |
| BC | ALA445 |
| BC | ARG449 |
| BC | CLA507 |
| BC | BCR515 |
| BI | PHE23 |
| site_id | AR5 |
| Number of Residues | 14 |
| Details | binding site for residue CLA BC 506 |
| Chain | Residue |
| BC | LEU161 |
| BC | LEU165 |
| BC | LEU213 |
| BC | ILE243 |
| BC | GLY247 |
| BC | TRP250 |
| BC | HIS251 |
| BC | THR255 |
| BC | PRO256 |
| BC | PHE257 |
| BC | TRP259 |
| BC | ALA260 |
| BC | PHE264 |
| BC | CLA507 |
| site_id | AR6 |
| Number of Residues | 13 |
| Details | binding site for residue CLA BC 507 |
| Chain | Residue |
| BC | MET157 |
| BC | LEU161 |
| BC | HIS164 |
| BC | ILE240 |
| BC | PHE264 |
| BC | TRP266 |
| BC | TYR271 |
| BC | TYR274 |
| BC | SER275 |
| BC | CLA505 |
| BC | CLA506 |
| BC | CLA509 |
| BC | BCR515 |
| site_id | AR7 |
| Number of Residues | 16 |
| Details | binding site for residue CLA BC 508 |
| Chain | Residue |
| BA | LHG412 |
| BC | TRP36 |
| BC | ALA37 |
| BC | ASN39 |
| BC | ALA40 |
| BC | GLU269 |
| BC | LEU276 |
| BC | PHE436 |
| BC | PHE437 |
| BC | GLY440 |
| BC | TRP443 |
| BC | HIS444 |
| BC | ARG447 |
| BC | CLA509 |
| BC | CLA510 |
| BK | VAL30 |
| site_id | AR8 |
| Number of Residues | 17 |
| Details | binding site for residue CLA BC 509 |
| Chain | Residue |
| BC | ASN39 |
| BC | LEU42 |
| BC | ILE43 |
| BC | LEU49 |
| BC | ALA52 |
| BC | HIS53 |
| BC | TYR149 |
| BC | TRP151 |
| BC | GLY268 |
| BC | LEU272 |
| BC | SER275 |
| BC | LEU279 |
| BC | CLA507 |
| BC | CLA508 |
| BC | CLA510 |
| BC | CLA511 |
| BC | CLA512 |
| site_id | AR9 |
| Number of Residues | 16 |
| Details | binding site for residue CLA BC 510 |
| Chain | Residue |
| BC | ASN39 |
| BC | HIS56 |
| BC | LEU59 |
| BC | ILE60 |
| BC | LEU279 |
| BC | PHE436 |
| BC | PHE437 |
| BC | CLA502 |
| BC | CLA503 |
| BC | CLA504 |
| BC | CLA508 |
| BC | CLA509 |
| BC | CLA511 |
| BK | PRO29 |
| BK | VAL30 |
| BK | LEU33 |
| site_id | AS1 |
| Number of Residues | 22 |
| Details | binding site for residue CLA BC 511 |
| Chain | Residue |
| BC | GLN28 |
| BC | TRP35 |
| BC | GLY38 |
| BC | ASN39 |
| BC | ARG41 |
| BC | LEU42 |
| BC | LYS48 |
| BC | ALA52 |
| BC | PHE127 |
| BC | ALA133 |
| BC | ILE134 |
| BC | CLA509 |
| BC | CLA510 |
| BC | BCR514 |
| BK | LEU33 |
| BK | TRP39 |
| BK | GLN40 |
| BZ | VAL20 |
| BZ | PRO24 |
| By | ILE35 |
| By | ASN45 |
| By | LEU46 |
| site_id | AS2 |
| Number of Residues | 15 |
| Details | binding site for residue CLA BC 512 |
| Chain | Residue |
| BC | HIS53 |
| BC | ALA57 |
| BC | PHE147 |
| BC | PHE163 |
| BC | HIS164 |
| BC | VAL167 |
| BC | LEU168 |
| BC | ILE170 |
| BC | GLY171 |
| BC | LEU174 |
| BC | CLA503 |
| BC | CLA509 |
| BC | CLA513 |
| BC | LMG520 |
| BZ | BCR101 |
| site_id | AS3 |
| Number of Residues | 12 |
| Details | binding site for residue CLA BC 513 |
| Chain | Residue |
| BC | LEU50 |
| BC | VAL54 |
| BC | GLY128 |
| BC | TYR131 |
| BC | HIS132 |
| BC | PRO137 |
| BC | LEU140 |
| BC | TYR143 |
| BC | PHE147 |
| BC | ILE170 |
| BC | CLA512 |
| BZ | BCR101 |
| site_id | AS4 |
| Number of Residues | 16 |
| Details | binding site for residue BCR BC 514 |
| Chain | Residue |
| BC | ALA55 |
| BC | GLY58 |
| BC | LEU59 |
| BC | VAL116 |
| BC | ILE120 |
| BC | SER122 |
| BC | ALA123 |
| BC | CLA511 |
| BK | TYR15 |
| BK | PHE18 |
| BK | PHE32 |
| BK | TRP39 |
| BK | BCR102 |
| BZ | LEU9 |
| BZ | VAL13 |
| BZ | BCR101 |
| site_id | AS5 |
| Number of Residues | 15 |
| Details | binding site for residue BCR BC 515 |
| Chain | Residue |
| BC | ILE209 |
| BC | PHE210 |
| BC | TYR212 |
| BC | LEU213 |
| BC | ASP232 |
| BC | VAL233 |
| BC | HIS237 |
| BC | ILE240 |
| BC | PHE264 |
| BC | CLA501 |
| BC | CLA505 |
| BC | CLA507 |
| BI | VAL20 |
| BI | PHE23 |
| BI | LEU24 |
| site_id | AS6 |
| Number of Residues | 19 |
| Details | binding site for residue DGD BC 516 |
| Chain | Residue |
| BA | LEU151 |
| BA | PHE155 |
| BA | ILE163 |
| BC | PRO217 |
| BC | PHE218 |
| BC | GLY219 |
| BC | GLY220 |
| BC | GLY222 |
| BC | VAL225 |
| BC | SER226 |
| BC | PHE284 |
| BC | CYS288 |
| BC | PHE292 |
| BC | ASN294 |
| BC | THR305 |
| BC | PRO307 |
| BC | PHE361 |
| BC | ARG362 |
| BC | LEU438 |
| site_id | AS7 |
| Number of Residues | 18 |
| Details | binding site for residue DGD BC 517 |
| Chain | Residue |
| BA | PHE197 |
| BC | TYR82 |
| BC | GLU83 |
| BC | GLN84 |
| BC | GLY85 |
| BC | LEU404 |
| BC | SER406 |
| BC | ASN418 |
| BC | VAL420 |
| BC | TRP425 |
| BC | THR428 |
| BC | SER429 |
| BC | CLA504 |
| BC | DGD518 |
| BC | LMG519 |
| BC | LHG521 |
| BJ | TYR33 |
| BJ | BCR102 |
| site_id | AS8 |
| Number of Residues | 20 |
| Details | binding site for residue DGD BC 518 |
| Chain | Residue |
| BA | LEU200 |
| BA | TRP278 |
| BA | PHE300 |
| BA | PHE302 |
| BA | SER305 |
| BA | SQD413 |
| BC | ASN405 |
| BC | ASN415 |
| BC | SER416 |
| BC | ASN418 |
| BC | CLA504 |
| BC | DGD517 |
| BJ | PHE29 |
| BJ | ALA32 |
| BJ | TYR33 |
| BJ | GLY37 |
| BJ | SER38 |
| BJ | SER39 |
| BJ | BCR102 |
| BV | GLN60 |
| site_id | AS9 |
| Number of Residues | 7 |
| Details | binding site for residue LMG BC 519 |
| Chain | Residue |
| BC | HIS74 |
| BC | CLA504 |
| BC | DGD517 |
| BJ | BCR102 |
| BK | ASP23 |
| BK | VAL30 |
| By | ILE25 |
| site_id | AT1 |
| Number of Residues | 10 |
| Details | binding site for residue LMG BC 520 |
| Chain | Residue |
| BC | TRP97 |
| BC | ASP107 |
| BC | PHE109 |
| BC | VAL113 |
| BC | VAL114 |
| BC | VAL117 |
| BC | HIS118 |
| BC | CLA503 |
| BC | CLA512 |
| BZ | PHE59 |
| site_id | AT2 |
| Number of Residues | 8 |
| Details | binding site for residue LHG BC 521 |
| Chain | Residue |
| BA | TYR262 |
| BA | ASN266 |
| BA | SQD413 |
| BC | TRP35 |
| BC | DGD517 |
| BE | LMG102 |
| BJ | BCR102 |
| BK | PHE45 |
| site_id | AT3 |
| Number of Residues | 8 |
| Details | binding site for residue BCT BD 401 |
| Chain | Residue |
| BA | HIS215 |
| BA | TYR246 |
| BA | HIS272 |
| BA | FE2402 |
| BD | HIS214 |
| BD | TYR244 |
| BD | LYS264 |
| BD | HIS268 |
| site_id | AT4 |
| Number of Residues | 23 |
| Details | binding site for residue CLA BD 402 |
| Chain | Residue |
| BA | PHE206 |
| BA | CLA403 |
| BA | CLA404 |
| BA | CLA405 |
| BD | TRP48 |
| BD | PRO149 |
| BD | VAL152 |
| BD | PHE153 |
| BD | VAL156 |
| BD | PHE181 |
| BD | LEU182 |
| BD | PHE185 |
| BD | GLN186 |
| BD | TRP191 |
| BD | THR192 |
| BD | HIS197 |
| BD | GLY200 |
| BD | VAL201 |
| BD | VAL204 |
| BD | LEU279 |
| BD | SER282 |
| BD | ALA283 |
| BD | PHO403 |
| site_id | AT5 |
| Number of Residues | 19 |
| Details | binding site for residue PHO BD 403 |
| Chain | Residue |
| BA | PHE206 |
| BA | LEU210 |
| BA | MET214 |
| BA | CLA405 |
| BD | LEU37 |
| BD | ALA41 |
| BD | TRP48 |
| BD | GLY118 |
| BD | LEU122 |
| BD | PHE125 |
| BD | ASN142 |
| BD | ALA145 |
| BD | PHE146 |
| BD | ALA148 |
| BD | PRO149 |
| BD | PHE153 |
| BD | PRO275 |
| BD | LEU279 |
| BD | CLA402 |
| site_id | AT6 |
| Number of Residues | 15 |
| Details | binding site for residue CLA BD 404 |
| Chain | Residue |
| BB | CLA611 |
| BD | LEU43 |
| BD | LEU89 |
| BD | LEU90 |
| BD | LEU91 |
| BD | LEU92 |
| BD | TRP93 |
| BD | TRP104 |
| BD | THR112 |
| BD | PHE113 |
| BD | HIS117 |
| BD | LMT411 |
| BX | GLY22 |
| BX | LEU23 |
| BX | GLY26 |
| site_id | AT7 |
| Number of Residues | 18 |
| Details | binding site for residue PL9 BD 405 |
| Chain | Residue |
| BA | PHE52 |
| BA | ILE53 |
| BA | ILE77 |
| BA | CLA404 |
| BD | MET199 |
| BD | ALA202 |
| BD | HIS214 |
| BD | THR217 |
| BD | TRP253 |
| BD | ALA260 |
| BD | PHE261 |
| BD | LEU267 |
| BD | PHE273 |
| BD | VAL274 |
| BD | THR277 |
| BD | LMG408 |
| BL | LEU23 |
| BL | VAL26 |
| site_id | AT8 |
| Number of Residues | 11 |
| Details | binding site for residue BCR BD 406 |
| Chain | Residue |
| BD | TYR42 |
| BD | GLY46 |
| BD | GLY47 |
| BD | LEU49 |
| BD | THR50 |
| BD | PHE101 |
| BF | PRO29 |
| BF | PHE33 |
| BJ | VAL21 |
| BJ | VAL25 |
| BJ | PL9101 |
| site_id | AT9 |
| Number of Residues | 11 |
| Details | binding site for residue LMG BD 407 |
| Chain | Residue |
| BA | CLA405 |
| BD | TYR67 |
| BD | GLY70 |
| BD | CYS71 |
| BD | PHE73 |
| BF | ILE37 |
| BF | MET40 |
| BF | GLN41 |
| BJ | GLY31 |
| BJ | ALA32 |
| BJ | GLY37 |
| site_id | AU1 |
| Number of Residues | 13 |
| Details | binding site for residue LMG BD 408 |
| Chain | Residue |
| BD | PHE257 |
| BD | ALA260 |
| BD | PHE261 |
| BD | SER262 |
| BD | ASN263 |
| BD | TRP266 |
| BD | PHE270 |
| BD | PL9405 |
| BL | THR15 |
| BL | TYR18 |
| BL | LEU19 |
| BT | PHE17 |
| BT | ALA20 |
| site_id | AU2 |
| Number of Residues | 9 |
| Details | binding site for residue SQD BD 409 |
| Chain | Residue |
| BB | LYS227 |
| BB | ALA228 |
| BB | ARG230 |
| BB | LEU474 |
| BB | LMT626 |
| BD | LYS23 |
| BD | TRP32 |
| BD | ARG134 |
| BD | LEU135 |
| site_id | AU3 |
| Number of Residues | 6 |
| Details | binding site for residue DGD BD 410 |
| Chain | Residue |
| BD | ASP100 |
| BD | PHE101 |
| BD | LMT411 |
| BE | LEU42 |
| BE | ASP45 |
| BE | VAL46 |
| site_id | AU4 |
| Number of Residues | 8 |
| Details | binding site for residue LMT BD 411 |
| Chain | Residue |
| BD | LEU92 |
| BD | TRP93 |
| BD | GLY99 |
| BD | CLA404 |
| BD | DGD410 |
| BX | ILE21 |
| BX | SER25 |
| BX | GLY26 |
| site_id | AU5 |
| Number of Residues | 14 |
| Details | binding site for residue HEM BE 101 |
| Chain | Residue |
| BE | ARG8 |
| BE | ILE13 |
| BE | ARG18 |
| BE | TYR19 |
| BE | HIS23 |
| BE | THR26 |
| BE | ILE27 |
| BE | LEU30 |
| BF | ILE15 |
| BF | ARG19 |
| BF | TRP20 |
| BF | HIS24 |
| BF | ALA27 |
| BF | ILE31 |
| site_id | AU6 |
| Number of Residues | 7 |
| Details | binding site for residue LMG BE 102 |
| Chain | Residue |
| BA | TYR262 |
| BC | LHG521 |
| BD | PHE27 |
| BE | PRO9 |
| BE | PHE10 |
| BE | SER11 |
| BJ | PL9101 |
| site_id | AU7 |
| Number of Residues | 8 |
| Details | binding site for residue SQD BF 101 |
| Chain | Residue |
| BD | TRP21 |
| BD | ARG24 |
| BD | ARG26 |
| BE | GLU7 |
| BF | PHE16 |
| BF | THR17 |
| BF | VAL18 |
| BX | THR33 |
| site_id | AU8 |
| Number of Residues | 14 |
| Details | binding site for residue DGD BH 101 |
| Chain | Residue |
| BB | TYR193 |
| BB | PHE250 |
| BB | TYR258 |
| BB | TYR273 |
| BB | SER277 |
| BB | PHE463 |
| BB | CLA605 |
| BD | HIS87 |
| BD | LEU116 |
| BD | SER165 |
| BH | TYR49 |
| BH | VAL60 |
| BH | SER61 |
| BH | TRP62 |
| site_id | AU9 |
| Number of Residues | 6 |
| Details | binding site for residue LMG BI 101 |
| Chain | Residue |
| AB | DGD626 |
| AB | LMT627 |
| BI | MET1 |
| BI | THR3 |
| BI | LEU4 |
| BI | LMT102 |
| site_id | AV1 |
| Number of Residues | 5 |
| Details | binding site for residue LMT BI 102 |
| Chain | Residue |
| BI | THR3 |
| BI | ILE6 |
| BI | ILE10 |
| BI | VAL11 |
| BI | LMG101 |
| site_id | AV2 |
| Number of Residues | 6 |
| Details | binding site for residue PL9 BJ 101 |
| Chain | Residue |
| BA | PL9408 |
| BA | SQD413 |
| BD | BCR406 |
| BE | LMG102 |
| BJ | VAL16 |
| BJ | GLY20 |
| site_id | AV3 |
| Number of Residues | 7 |
| Details | binding site for residue BCR BJ 102 |
| Chain | Residue |
| BC | DGD517 |
| BC | DGD518 |
| BC | LMG519 |
| BC | LHG521 |
| BJ | PHE29 |
| BJ | TYR33 |
| BK | BCR102 |
| site_id | AV4 |
| Number of Residues | 2 |
| Details | binding site for residue CA BK 101 |
| Chain | Residue |
| BK | ASP19 |
| BK | ASP23 |
| site_id | AV5 |
| Number of Residues | 18 |
| Details | binding site for residue BCR BK 102 |
| Chain | Residue |
| BC | BCR514 |
| BJ | ALA14 |
| BJ | THR15 |
| BJ | GLY18 |
| BJ | MET19 |
| BJ | BCR102 |
| BK | LEU21 |
| BK | LEU25 |
| BK | LEU31 |
| BK | PHE32 |
| BK | PHE37 |
| BK | VAL38 |
| BK | ALA41 |
| BZ | VAL13 |
| BZ | SER16 |
| By | ILE28 |
| By | GLY29 |
| By | GLY32 |
| site_id | AV6 |
| Number of Residues | 9 |
| Details | binding site for residue SQD BL 101 |
| Chain | Residue |
| AB | ARG18 |
| AB | LEU29 |
| AB | SER104 |
| AB | BCR617 |
| AL | ASN4 |
| BL | ARG14 |
| BL | TYR18 |
| BM | TYR26 |
| BT | PHE23 |
| site_id | AV7 |
| Number of Residues | 4 |
| Details | binding site for residue LMT BM 101 |
| Chain | Residue |
| AM | MET1 |
| BB | TYR40 |
| BB | LMG624 |
| BM | GLN5 |
| site_id | AV8 |
| Number of Residues | 8 |
| Details | binding site for residue LMG BM 102 |
| Chain | Residue |
| AB | CLA614 |
| AL | VAL10 |
| AM | ILE24 |
| AM | GLN32 |
| BM | ILE23 |
| BM | GLU30 |
| BM | SER31 |
| BM | GLN33 |
| site_id | AV9 |
| Number of Residues | 3 |
| Details | binding site for residue CA BO 301 |
| Chain | Residue |
| BO | GLU81 |
| BO | GLU140 |
| BO | HIS257 |
| site_id | AW1 |
| Number of Residues | 5 |
| Details | binding site for residue LMT BT 101 |
| Chain | Residue |
| AB | SER36 |
| AB | ALA43 |
| AB | LMG623 |
| BA | LEU72 |
| BT | VAL7 |
| site_id | AW2 |
| Number of Residues | 14 |
| Details | binding site for residue HEM BV 201 |
| Chain | Residue |
| BV | ALA62 |
| BV | CYS63 |
| BV | CYS66 |
| BV | HIS67 |
| BV | THR74 |
| BV | LEU78 |
| BV | ASP79 |
| BV | THR84 |
| BV | LEU85 |
| BV | ALA88 |
| BV | TYR101 |
| BV | MET102 |
| BV | TYR108 |
| BV | HIS118 |
| site_id | AW3 |
| Number of Residues | 8 |
| Details | binding site for residue BCR BX 101 |
| Chain | Residue |
| BB | CLA604 |
| BB | CLA612 |
| BH | MET35 |
| BH | PHE38 |
| BH | PHE41 |
| BX | THR11 |
| BX | ILE12 |
| BX | LEU16 |
| site_id | AW4 |
| Number of Residues | 11 |
| Details | binding site for residue BCR BZ 101 |
| Chain | Residue |
| BC | PHE112 |
| BC | VAL116 |
| BC | VAL124 |
| BC | LEU125 |
| BC | CLA512 |
| BC | CLA513 |
| BC | BCR514 |
| BK | TYR15 |
| BZ | VAL54 |
| BZ | GLY55 |
| BZ | ASN58 |
Functional Information from PROSITE/UniProt
| site_id | PS00244 |
| Number of Residues | 27 |
| Details | REACTION_CENTER Photosynthetic reaction center proteins signature. NwtlnPfHmmGvagvlggallcAiHGA |
| Chain | Residue | Details |
| AD | ASN190-ALA216 | |
| AA | ASN191-SER217 |
| site_id | PS00537 |
| Number of Residues | 15 |
| Details | CYTOCHROME_B559 Cytochrome b559 subunits heme-binding site signature. ItSVRYwvIHSITIP |
| Chain | Residue | Details |
| AE | ILE14-PRO28 | |
| AF | ILE15-PRO29 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 470 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 840 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 216 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Site: {"description":"Tyrosine radical intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11217865","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Site: {"description":"Stabilizes free radical intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 258 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 452 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 92 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01496","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 664 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 474 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 246 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI23 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI24 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI25 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI26 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI27 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI28 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_00642","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI29 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_00643","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"16172937","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI30 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI31 |
| Number of Residues | 28 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI32 |
| Number of Residues | 26 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI33 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00808","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI34 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"12881497","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgangb K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/b406989g"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI35 |
| Number of Residues | 6 |
| Details | Topological domain: {"description":"Lumenal"} |
| Chain | Residue | Details |






